作者: Georgianna Sandeen , William I. Wood , Gary Felsenfeld
关键词: Linker DNA 、 Histone 、 HMGN 、 High-mobility group 、 Biochemistry 、 DNA 、 Nuclease 、 Nucleosome 、 Biophysics 、 Biology 、 Hmg protein
摘要: The interaction of the high mobility group proteins, HMG14 and HMG17, with nucleosome core particles has been studied. results show that two molecules HMG14/17 can be bound tightly but reversibly to each particle their affinity for is greater than histone-free DNA size. Thermal denaturation nuclease digestion studies suggest major sites are located near ends DNA. When preparations from chicken erythrocyte nuclei stripped HMG proteins partially titrated HMG14/17, nucleosome-HMG complex fraction enriched in beta-globin gene sequences.